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Protein

mRNA-capping enzyme subunit alpha

Gene

CEG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.

Catalytic activityi

GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.

Cofactori

a divalent metal cationNote: Divalent metal ions.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei70N6-GMP-lysine intermediate1 Publication1

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • mRNA guanylyltransferase activity Source: SGD

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • tRNA processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30626-MONOMER.
YEAST:G3O-30626-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme subunit alpha
Alternative name(s):
GTP--RNA guanylyltransferase
Short name:
GTase
mRNA guanylyltransferase (EC:2.7.7.50)
Gene namesi
Name:CEG1
Ordered Locus Names:YGL130W
ORF Names:G2853
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL130W.
SGDiS000003098. CEG1.

Subcellular locationi

GO - Cellular componenti

  • mRNA cap methyltransferase complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi57E → A: No effect. 1 Publication1
Mutagenesisi58E → A: No effect. 1 Publication1
Mutagenesisi59K → A, T, S or R: No effect. 1 Publication1
Mutagenesisi66Y → A: Temperature-sensitive. 1 Publication1
Mutagenesisi70K → A, R, M, I or T: Lethal. 1 Publication1
Mutagenesisi71T → A: No effect. 1 Publication1
Mutagenesisi72D → A: No effect. 1 Publication1
Mutagenesisi73G → A: Lethal. 1 Publication1
Mutagenesisi95D → A: Temperature-sensitive. 1 Publication1
Mutagenesisi96R → A: Temperature-sensitive. 1 Publication1
Mutagenesisi97E → A: Temperature-sensitive. 1 Publication1
Mutagenesisi107 – 109RFP → AAA: Reduced growth at 25 degrees and lethal at 37 degrees. 1 Publication3
Mutagenesisi114K → A: No effect. 1 Publication1
Mutagenesisi115K → A: No effect. 1 Publication1
Mutagenesisi116K → A: No effect. 1 Publication1
Mutagenesisi117E → A: No effect. 1 Publication1
Mutagenesisi118E → A: No effect. 1 Publication1
Mutagenesisi129L → A: No effect. 1 Publication1
Mutagenesisi130D → A: Lethal. 1 Publication1
Mutagenesisi131G → A: Temperature-sensitive. 1 Publication1
Mutagenesisi132E → A: Lethal. 1 Publication1
Mutagenesisi134V → A: No effect. 1 Publication1
Mutagenesisi218D → A: No effect. 1 Publication1
Mutagenesisi219K → A: No effect. 1 Publication1
Mutagenesisi225D → A: Lethal. 1 Publication1
Mutagenesisi226G → A: Lethal. 1 Publication1
Mutagenesisi241K → A: No effect. 1 Publication1
Mutagenesisi242D → A: No effect. 1 Publication1
Mutagenesisi249K → A: Lethal. 1 Publication1
Mutagenesisi253E → A: No effect. 1 Publication1
Mutagenesisi254N → A: No effect. 1 Publication1
Mutagenesisi255T → A: Temperature-sensitive. 1 Publication1
Mutagenesisi257D → A: Lethal. 1 Publication1
Mutagenesisi274K → A: No effect. 1 Publication1
Mutagenesisi275D → A: No effect. 1 Publication1
Mutagenesisi276D → A: No effect. 1 Publication1
Mutagenesisi395E → A: No effect. 1 Publication1
Mutagenesisi396D → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101061 – 459mRNA-capping enzyme subunit alphaAdd BLAST459

Proteomic databases

MaxQBiQ01159.
PRIDEiQ01159.

PTM databases

iPTMnetiQ01159.

Interactioni

Subunit structurei

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.

Binary interactionsi

WithEntry#Exp.IntActNotes
CET1O132977EBI-10503,EBI-4473

Protein-protein interaction databases

BioGridi33121. 86 interactors.
DIPiDIP-2298N.
IntActiQ01159. 26 interactors.
MINTiMINT-621589.

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 33Combined sources13
Helixi38 – 40Combined sources3
Beta strandi47 – 50Combined sources4
Helixi53 – 58Combined sources6
Beta strandi61 – 63Combined sources3
Beta strandi65 – 71Combined sources7
Beta strandi73 – 82Combined sources10
Turni84 – 86Combined sources3
Beta strandi89 – 94Combined sources6
Beta strandi96 – 98Combined sources3
Beta strandi100 – 103Combined sources4
Helixi118 – 120Combined sources3
Beta strandi126 – 137Combined sources12
Turni139 – 141Combined sources3
Beta strandi144 – 156Combined sources13
Beta strandi162 – 165Combined sources4
Helixi166 – 175Combined sources10
Helixi178 – 187Combined sources10
Beta strandi197 – 201Combined sources5
Helixi207 – 209Combined sources3
Helixi210 – 217Combined sources8
Beta strandi224 – 235Combined sources12
Beta strandi238 – 247Combined sources10
Turni251 – 253Combined sources3
Beta strandi257 – 261Combined sources5
Beta strandi291 – 295Combined sources5
Helixi300 – 307Combined sources8
Turni313 – 316Combined sources4
Helixi317 – 320Combined sources4
Turni321 – 323Combined sources3
Beta strandi324 – 329Combined sources6
Turni334 – 336Combined sources3
Helixi337 – 342Combined sources6
Beta strandi350 – 354Combined sources5
Turni358 – 360Combined sources3
Beta strandi365 – 368Combined sources4
Beta strandi372 – 374Combined sources3
Helixi378 – 390Combined sources13
Helixi395 – 398Combined sources4
Helixi399 – 401Combined sources3
Helixi402 – 414Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KYHX-ray3.00C/D1-459[»]
ProteinModelPortaliQ01159.
SMRiQ01159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01159.

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

HOGENOMiHOG000162728.
InParanoidiQ01159.
KOiK00987.
OMAiKPPEENT.
OrthoDBiEOG092C2LUY.

Family and domain databases

InterProiIPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR017075. mRNA_capping_enz_asu.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Q01159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLAMESRVA PEIPGLIQPG NVTQDLKMMV CKLLNSPKPT KTFPGSQPVS
60 70 80 90 100
FQHSDVEEKL LAHDYYVCEK TDGLRVLMFI VINPVTGEQG CFMIDRENNY
110 120 130 140 150
YLVNGFRFPR LPQKKKEELL ETLQDGTLLD GELVIQTNPM TKLQELRYLM
160 170 180 190 200
FDCLAINGRC LTQSPTSSRL AHLGKEFFKP YFDLRAAYPN RCTTFPFKIS
210 220 230 240 250
MKHMDFSYQL VKVAKSLDKL PHLSDGLIFT PVKAPYTAGG KDSLLLKWKP
260 270 280 290 300
EQENTVDFKL ILDIPMVEDP SLPKDDRNRW YYNYDVKPVF SLYVWQGGAD
310 320 330 340 350
VNSRLKHFDQ PFDRKEFEIL ERTYRKFAEL SVSDEEWQNL KNLEQPLNGR
360 370 380 390 400
IVECAKNQET GAWEMLRFRD DKLNGNHTSV VQKVLESIND SVSLEDLEEI
410 420 430 440 450
VGDIKRCWDE RRANMAGGSG RPLPSQSQNA TLSTSKPVHS QPPSNDKEPK

YVDEDDWSD
Length:459
Mass (Da):52,764
Last modified:February 1, 1995 - v2
Checksum:iF7F5A3E59EEFA15F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45G → S (PubMed:7500935).Curated1
Sequence conflicti300D → N (PubMed:7500935).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10263 Genomic DNA. Translation: BAA01103.1.
X87252 Genomic DNA. Translation: CAA60705.1.
Z72652 Genomic DNA. Translation: CAA96839.1.
BK006941 Genomic DNA. Translation: DAA07979.1.
PIRiS59731.
RefSeqiNP_011385.3. NM_001180995.3.

Genome annotation databases

EnsemblFungiiYGL130W; YGL130W; YGL130W.
GeneIDi852747.
KEGGisce:YGL130W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10263 Genomic DNA. Translation: BAA01103.1.
X87252 Genomic DNA. Translation: CAA60705.1.
Z72652 Genomic DNA. Translation: CAA96839.1.
BK006941 Genomic DNA. Translation: DAA07979.1.
PIRiS59731.
RefSeqiNP_011385.3. NM_001180995.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KYHX-ray3.00C/D1-459[»]
ProteinModelPortaliQ01159.
SMRiQ01159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33121. 86 interactors.
DIPiDIP-2298N.
IntActiQ01159. 26 interactors.
MINTiMINT-621589.

PTM databases

iPTMnetiQ01159.

Proteomic databases

MaxQBiQ01159.
PRIDEiQ01159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL130W; YGL130W; YGL130W.
GeneIDi852747.
KEGGisce:YGL130W.

Organism-specific databases

EuPathDBiFungiDB:YGL130W.
SGDiS000003098. CEG1.

Phylogenomic databases

HOGENOMiHOG000162728.
InParanoidiQ01159.
KOiK00987.
OMAiKPPEENT.
OrthoDBiEOG092C2LUY.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30626-MONOMER.
YEAST:G3O-30626-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ01159.
PROiQ01159.

Family and domain databases

InterProiIPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR017075. mRNA_capping_enz_asu.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMCE1_YEAST
AccessioniPrimary (citable) accession number: Q01159
Secondary accession number(s): D6VU18, Q9URD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 279 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.